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Database: UniProt
Entry: A0A498LC33_LABRO
LinkDB: A0A498LC33_LABRO
Original site: A0A498LC33_LABRO 
ID   A0A498LC33_LABRO        Unreviewed;       627 AA.
AC   A0A498LC33;
DT   05-JUN-2019, integrated into UniProtKB/TrEMBL.
DT   05-JUN-2019, sequence version 1.
DT   24-JAN-2024, entry version 14.
DE   SubName: Full=SPARC 1 {ECO:0000313|EMBL:RXN04476.1};
GN   ORFNames=ROHU_035708 {ECO:0000313|EMBL:RXN04476.1};
OS   Labeo rohita (Indian major carp) (Cyprinus rohita).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC   Cyprinidae; Labeoninae; Labeonini; Labeo.
OX   NCBI_TaxID=84645 {ECO:0000313|EMBL:RXN04476.1, ECO:0000313|Proteomes:UP000290572};
RN   [1] {ECO:0000313|EMBL:RXN04476.1, ECO:0000313|Proteomes:UP000290572}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DASCIFA01 {ECO:0000313|EMBL:RXN04476.1};
RC   TISSUE=Testis {ECO:0000313|EMBL:RXN04476.1};
RA   Das P., Kushwaha B., Joshi C.G., Kumar D., Nagpure N.S., Sahoo L.,
RA   Das S.P., Bit A., Patnaik S., Meher P.K., Jayasankar P., Koringa P.G.,
RA   Patel N.V., Hinsu A.T., Kumar R., Pandey M., Agarwal S., Srivastava S.,
RA   Singh M., Iquebal M.A., Jaiswal S., Angadi U.B., Kumar N., Raza M.,
RA   Shah T.M., Rai A., Jena J.K.;
RT   "Draft genome sequence of Rohu Carp (Labeo rohita).";
RL   Submitted (MAR-2018) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the SPARC family.
CC       {ECO:0000256|ARBA:ARBA00006404}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:RXN04476.1}.
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DR   EMBL; QBIY01013442; RXN04476.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A498LC33; -.
DR   STRING; 84645.A0A498LC33; -.
DR   Proteomes; UP000290572; Unassembled WGS sequence.
DR   GO; GO:0005615; C:extracellular space; IEA:InterPro.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR   Gene3D; 3.30.60.30; -; 1.
DR   Gene3D; 1.10.238.10; EF-hand; 1.
DR   InterPro; IPR011992; EF-hand-dom_pair.
DR   InterPro; IPR018247; EF_Hand_1_Ca_BS.
DR   InterPro; IPR003645; Fol_N.
DR   InterPro; IPR015369; Follistatin/Osteonectin_EGF.
DR   InterPro; IPR002350; Kazal_dom.
DR   InterPro; IPR036058; Kazal_dom_sf.
DR   InterPro; IPR001999; Osteonectin_CS.
DR   InterPro; IPR019577; SPARC/Testican_Ca-bd-dom.
DR   PANTHER; PTHR13866; SPARC OSTEONECTIN; 1.
DR   PANTHER; PTHR13866:SF25; SPARC-LIKE 1; 1.
DR   Pfam; PF09289; FOLN; 1.
DR   Pfam; PF07648; Kazal_2; 1.
DR   Pfam; PF10591; SPARC_Ca_bdg; 1.
DR   SMART; SM00274; FOLN; 1.
DR   SMART; SM00280; KAZAL; 1.
DR   SUPFAM; SSF47473; EF-hand; 1.
DR   SUPFAM; SSF57196; EGF/Laminin; 1.
DR   SUPFAM; SSF100895; Kazal-type serine protease inhibitors; 1.
DR   PROSITE; PS00018; EF_HAND_1; 1.
DR   PROSITE; PS51465; KAZAL_2; 1.
DR   PROSITE; PS00612; OSTEONECTIN_1; 1.
DR   PROSITE; PS00613; OSTEONECTIN_2; 1.
PE   3: Inferred from homology;
KW   Calcium {ECO:0000256|ARBA:ARBA00022837};
KW   Extracellular matrix {ECO:0000256|ARBA:ARBA00022530};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000290572};
KW   Secreted {ECO:0000256|ARBA:ARBA00022525};
KW   Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           22..627
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5019769449"
FT   DOMAIN          417..474
FT                   /note="Kazal-like"
FT                   /evidence="ECO:0000259|PROSITE:PS51465"
FT   REGION          22..199
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          212..356
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        31..51
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        75..95
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        132..173
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        251..284
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        292..314
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        326..355
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   627 AA;  71704 MW;  B8F1BE2D7E02EEB4 CRC64;
     MKKDLFLFCF LVSALAAYVQ SKPHGKNQHV KHNPTPKEQS ESVKHHDSKD GVLPTFLPFE
     SSTQDPEDED TSEENESRVE MKQAGAEEIK GSEEGEKNTP LLLSEEALTQ LLQVPEEADE
     PVQEDEDDGD SPEKDKEIKK MEEKKKDGES TMKNEDGTEQ REGENKVEDA NETDSSTESE
     IPMDLDYAAD RDASQPLPVK IEEAKASTIN TIKEVEETAE DVIPTVTVDY DSQQSNTDSE
     DTAEEQEVPA EQTQDELKEA FRDSEDVNEK EKSDQQDEKN SSGKKTKKEK KKQKNESNSH
     GKGKAKKQRN NQRMEKMQND QAGTMEETAE HTHRKDPEEL AEPIENTEPK AKRKNGKWTR
     LVGMNPVQIR ATMELYPDIR PTHRPSGQGL EADPCENFPC KRGKTCKMND ENKPVCVCQE
     PSECPPSVND FEHVCGTDNK TYDTSCQLFA TKCGLEGTKI GHRLHLDYTG SCKFIPPCLE
     SELVQFPLRM RDWLKNVLLQ LYEHESMSPG FLTAKQRIRV QKIYESERRL HAGDHPVELL
     QQDFEKNYNM YIYPVHWQFA QMDQHPSDRF LSHSELAPLR VPLVPMEHCT SVFFQKCDAD
     KDKLVSFKEW CICFGMKEED MDTNLLF
//
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